Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Nitrogen regulatory protein P-II 2

Gene

glnK

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

P-II indirectly controls the transcription of the glutamine synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of GlnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase by GlnE, so activating the enzyme (By similarity).By similarity

GO - Molecular functioni

  • enzyme regulator activity Source: InterPro
  • identical protein binding Source: IntAct
  • nucleotide binding Source: UniProtKB-KW

GO - Biological processi

  • positive regulation of nitrogen utilization Source: EcoCyc
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:PROTEIN-PII2.
ECOL316407:JW0440-MONOMER.
MetaCyc:PROTEIN-PII2.

Names & Taxonomyi

Protein namesi
Recommended name:
Nitrogen regulatory protein P-II 2
Gene namesi
Name:glnK
Synonyms:ybaI
Ordered Locus Names:b0450, JW0440
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12191. glnK.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 112112Nitrogen regulatory protein P-II 2PRO_0000139772Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei51 – 511O-UMP-tyrosinePROSITE-ProRule annotation

Post-translational modificationi

Uridylylated/deuridylylated by GlnD.

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP0AC55.
PaxDbiP0AC55.
PRIDEiP0AC55.

2D gel databases

SWISS-2DPAGEP0AC55.

Interactioni

Subunit structurei

Homotrimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-559503,EBI-559503
glnBP0A9Z13EBI-559503,EBI-551053
glnDP272493EBI-559503,EBI-552032
glnLP0AFB55EBI-559503,EBI-701156

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4263149. 10 interactions.
DIPiDIP-35006N.
IntActiP0AC55. 14 interactions.
MINTiMINT-1309225.
STRINGi511145.b0450.

Structurei

Secondary structure

112
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1 – 88Combined sources
Helixi10 – 123Combined sources
Helixi13 – 2210Combined sources
Beta strandi29 – 357Combined sources
Beta strandi37 – 393Combined sources
Beta strandi44 – 463Combined sources
Beta strandi49 – 513Combined sources
Beta strandi56 – 6611Combined sources
Helixi67 – 693Combined sources
Helixi70 – 8112Combined sources
Beta strandi84 – 863Combined sources
Beta strandi90 – 978Combined sources
Turni102 – 1043Combined sources
Helixi108 – 1114Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GNKX-ray2.00A/B1-112[»]
2GNKX-ray2.00A1-112[»]
2NS1X-ray1.96B1-112[»]
2NUUX-ray2.50G/H/I/J/K/L1-112[»]
ProteinModelPortaliP0AC55.
SMRiP0AC55. Positions 1-112.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AC55.

Family & Domainsi

Sequence similaritiesi

Belongs to the P(II) protein family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4108YZA. Bacteria.
COG0347. LUCA.
HOGENOMiHOG000017847.
InParanoidiP0AC55.
KOiK04752.
OMAiEMVEPAI.
OrthoDBiEOG69GZGV.
PhylomeDBiP0AC55.

Family and domain databases

Gene3Di3.30.70.120. 1 hit.
InterProiIPR002187. N-reg_PII.
IPR011322. N-reg_PII-like_a/b.
IPR015867. N-reg_PII/ATP_PRibTrfase_C.
IPR017918. N-reg_PII_CS.
IPR002332. N-reg_PII_urydylation_site.
[Graphical view]
PfamiPF00543. P-II. 1 hit.
[Graphical view]
PIRSFiPIRSF039144. GlnB. 1 hit.
PRINTSiPR00340. PIIGLNB.
SMARTiSM00938. P-II. 1 hit.
[Graphical view]
SUPFAMiSSF54913. SSF54913. 1 hit.
PROSITEiPS00638. PII_GLNB_CTER. 1 hit.
PS51343. PII_GLNB_DOM. 1 hit.
PS00496. PII_GLNB_UMP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AC55-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLVTVIIKP FKLEDVREAL SSIGIQGLTV TEVKGFGRQK GHAELYRGAE
60 70 80 90 100
YSVNFLPKVK IDVAIADDQL DEVIDIVSKA AYTGKIGDGK IFVAELQRVI
110
RIRTGEADEA AL
Length:112
Mass (Da):12,259
Last modified:November 8, 2005 - v1
Checksum:i1875CD92C162B537
GO

Sequence cautioni

The sequence AAB40206.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U40429 Genomic DNA. Translation: AAD14836.1.
S79842 Genomic DNA. Translation: AAA87955.1.
U82664 Genomic DNA. Translation: AAB40206.1. Different initiation.
U00096 Genomic DNA. Translation: AAC73553.1.
AP009048 Genomic DNA. Translation: BAE76230.1.
PIRiB64775.
RefSeqiNP_414984.1. NC_000913.3.
WP_000780338.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73553; AAC73553; b0450.
BAE76230; BAE76230; BAE76230.
GeneIDi945087.
KEGGiecj:JW0440.
eco:b0450.
PATRICi32116055. VBIEscCol129921_0469.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U40429 Genomic DNA. Translation: AAD14836.1.
S79842 Genomic DNA. Translation: AAA87955.1.
U82664 Genomic DNA. Translation: AAB40206.1. Different initiation.
U00096 Genomic DNA. Translation: AAC73553.1.
AP009048 Genomic DNA. Translation: BAE76230.1.
PIRiB64775.
RefSeqiNP_414984.1. NC_000913.3.
WP_000780338.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GNKX-ray2.00A/B1-112[»]
2GNKX-ray2.00A1-112[»]
2NS1X-ray1.96B1-112[»]
2NUUX-ray2.50G/H/I/J/K/L1-112[»]
ProteinModelPortaliP0AC55.
SMRiP0AC55. Positions 1-112.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263149. 10 interactions.
DIPiDIP-35006N.
IntActiP0AC55. 14 interactions.
MINTiMINT-1309225.
STRINGi511145.b0450.

2D gel databases

SWISS-2DPAGEP0AC55.

Proteomic databases

EPDiP0AC55.
PaxDbiP0AC55.
PRIDEiP0AC55.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73553; AAC73553; b0450.
BAE76230; BAE76230; BAE76230.
GeneIDi945087.
KEGGiecj:JW0440.
eco:b0450.
PATRICi32116055. VBIEscCol129921_0469.

Organism-specific databases

EchoBASEiEB2108.
EcoGeneiEG12191. glnK.

Phylogenomic databases

eggNOGiENOG4108YZA. Bacteria.
COG0347. LUCA.
HOGENOMiHOG000017847.
InParanoidiP0AC55.
KOiK04752.
OMAiEMVEPAI.
OrthoDBiEOG69GZGV.
PhylomeDBiP0AC55.

Enzyme and pathway databases

BioCyciEcoCyc:PROTEIN-PII2.
ECOL316407:JW0440-MONOMER.
MetaCyc:PROTEIN-PII2.

Miscellaneous databases

EvolutionaryTraceiP0AC55.
PROiP0AC55.

Family and domain databases

Gene3Di3.30.70.120. 1 hit.
InterProiIPR002187. N-reg_PII.
IPR011322. N-reg_PII-like_a/b.
IPR015867. N-reg_PII/ATP_PRibTrfase_C.
IPR017918. N-reg_PII_CS.
IPR002332. N-reg_PII_urydylation_site.
[Graphical view]
PfamiPF00543. P-II. 1 hit.
[Graphical view]
PIRSFiPIRSF039144. GlnB. 1 hit.
PRINTSiPR00340. PIIGLNB.
SMARTiSM00938. P-II. 1 hit.
[Graphical view]
SUPFAMiSSF54913. SSF54913. 1 hit.
PROSITEiPS00638. PII_GLNB_CTER. 1 hit.
PS51343. PII_GLNB_DOM. 1 hit.
PS00496. PII_GLNB_UMP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "An additional PII in Escherichia coli: a new regulatory protein in the glutamine synthetase cascade."
    Vanheeswijk W.C., Stegeman B., Hoving S., Molenaar D., Kahn D., Westerhoff H.V.
    FEMS Microbiol. Lett. 132:153-157(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. "Sequence of minutes 4-25 of Escherichia coli."
    Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Cloning and organization of the abc and mdl genes of Escherichia coli: relationship to eukaryotic multidrug resistance."
    Allikmets R., Gerrard B.C., Court D., Dean M.C.
    Gene 136:231-236(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  6. "An alternative PII protein in the regulation of glutamine synthetase in Escherichia coli."
    van Heeswijk W.C., Hoving S., Molenaar D., Stegeman B., Kahn D., Westerhoff H.V.
    Mol. Microbiol. 21:133-146(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  7. "GlnK, a PII-homologue: structure reveals ATP binding site and indicates how the T-loops may be involved in molecular recognition."
    Xu Y., Cheah E., Carr P.D., van Heeswijk W.C., Westerhoff H.V., Vasudevan S.G., Ollis D.L.
    J. Mol. Biol. 282:149-165(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Entry informationi

Entry nameiGLNK_ECOLI
AccessioniPrimary (citable) accession number: P0AC55
Secondary accession number(s): P38504, P77118, Q2MBX6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: March 16, 2016
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.